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Results 1 - 10 of 19 > >>
EC Number
Amino acid exchange
Commentary
Reference
A38V
the mutation significantly increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
A38V/S388N
the mutation increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
C130A
FAD binding site, FAD covalently attached
E247A
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
H70A
FAD binding site, FAD covalently attached
H70A/C130A
no activity, lack of essential FAD cofactor
Q353A
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q353N
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q384A
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q384N
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Results 1 - 10 of 19 > >>